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1l4x

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[[Image:1l4x.gif|left|200px]]
 
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==octameric de novo designed peptide==
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The line below this paragraph, containing "STRUCTURE_1l4x", creates the "Structure Box" on the page.
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<StructureSection load='1l4x' size='340' side='right'caption='[[1l4x]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1l4x]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4X FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4x OCA], [https://pdbe.org/1l4x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4x RCSB], [https://www.ebi.ac.uk/pdbsum/1l4x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4x ProSAT]</span></td></tr>
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{{STRUCTURE_1l4x| PDB=1l4x | SCENE= }}
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</table>
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<div style="background-color:#fffaf0;">
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'''octameric de novo designed peptide'''
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== Publication Abstract from PubMed ==
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==Overview==
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Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions.
Alpha-helical coiled coils represent a common protein oligomerization motif that are mainly stabilized by hydrophobic interactions occurring along their coiled-coil interface, the so-called hydrophobic seam. We have recently de novo designed and optimized a series of two-heptad repeat long coiled-coil peptides which are further stabilized by a complex network of inter- and intrahelical salt bridges. Here we have extended the de novo design of such two heptad-repeat long peptides by removing the central and most important g-e' Arg to Glu (g-e'RE) ionic interhelical interaction and replacing these residues by alanine residues. The effect of the missing interhelical ionic interaction on coiled-coil formation and stability has been analyzed by CD spectroscopy, analytical ultracentrifugation, and X-ray crystallography. We show that the peptide, while being highly alpha-helical, is no longer able to form a parallel coiled-coil structure but rather assumes an octameric globular helical assembly devoid of any coiled-coil interactions.
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==About this Structure==
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Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide.,Meier M, Lustig A, Aebi U, Burkhard P J Struct Biol. 2002 Jan-Feb;137(1-2):65-72. PMID:12064934<ref>PMID:12064934</ref>
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4X OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Removing an interhelical salt bridge abolishes coiled-coil formation in a de novo designed peptide., Meier M, Lustig A, Aebi U, Burkhard P, J Struct Biol. 2002 Jan-Feb;137(1-2):65-72. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12064934 12064934]
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</div>
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[[Category: Aebi, U.]]
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<div class="pdbe-citations 1l4x" style="background-color:#fffaf0;"></div>
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[[Category: Burkhard, P.]]
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== References ==
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[[Category: Lustig, A.]]
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<references/>
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[[Category: Meier, M.]]
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__TOC__
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[[Category: Coiled coil]]
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</StructureSection>
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[[Category: Ionic interaction]]
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[[Category: Large Structures]]
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[[Category: Protein de novo design]]
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[[Category: Aebi U]]
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[[Category: Protein folding]]
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[[Category: Burkhard P]]
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[[Category: Protein oligomerization]]
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[[Category: Lustig A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:36 2008''
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[[Category: Meier M]]

Current revision

octameric de novo designed peptide

PDB ID 1l4x

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